1e58: Difference between revisions
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|PDB= 1e58 |SIZE=350|CAPTION= <scene name='initialview01'>1e58</scene>, resolution 1.25Å | |PDB= 1e58 |SIZE=350|CAPTION= <scene name='initialview01'>1e58</scene>, resolution 1.25Å | ||
|SITE= <scene name='pdbsite=HIS:Phosphohistidine'>HIS</scene> | |SITE= <scene name='pdbsite=HIS:Phosphohistidine'>HIS</scene> | ||
|LIGAND= <scene name='pdbligand= | |LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NEP:N1-PHOSPHONOHISTIDINE'>NEP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> | ||
|ACTIVITY= [http://en.wikipedia.org/wiki/Phosphoglycerate_mutase Phosphoglycerate mutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.2.1 5.4.2.1] | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphoglycerate_mutase Phosphoglycerate mutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.2.1 5.4.2.1] </span> | ||
|GENE= PGM1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | |GENE= PGM1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1e58 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e58 OCA], [http://www.ebi.ac.uk/pdbsum/1e58 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1e58 RCSB]</span> | |||
}} | }} | ||
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[[Category: Bond, C S.]] | [[Category: Bond, C S.]] | ||
[[Category: Hunter, W N.]] | [[Category: Hunter, W N.]] | ||
[[Category: glycolysis and gluconeogenesis]] | [[Category: glycolysis and gluconeogenesis]] | ||
[[Category: isomerase]] | [[Category: isomerase]] | ||
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[[Category: phosphohistidine]] | [[Category: phosphohistidine]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:55:29 2008'' | ||
Revision as of 19:55, 30 March 2008
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| , resolution 1.25Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | , , | ||||||
| Gene: | PGM1 (Escherichia coli) | ||||||
| Activity: | Phosphoglycerate mutase, with EC number 5.4.2.1 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
E.COLI COFACTOR-DEPENDENT PHOSPHOGLYCERATE MUTASE
OverviewOverview
The active conformation of the dimeric cofactor-dependent phosphoglycerate mutase (dPGM) from Escherichia coli has been elucidated by crystallographic methods to a resolution of 1.25 A (R-factor 0.121; R-free 0.168). The active site residue His(10), central in the catalytic mechanism of dPGM, is present as a phosphohistidine with occupancy of 0.28. The structural changes on histidine phosphorylation highlight various features that are significant in the catalytic mechanism. The C-terminal 10-residue tail, which is not observed in previous dPGM structures, is well ordered and interacts with residues implicated in substrate binding; the displacement of a loop adjacent to the active histidine brings previously overlooked residues into positions where they may directly influence catalysis. E. coli dPGM, like the mammalian dPGMs, is a dimer, whereas previous structural work has concentrated on monomeric and tetrameric yeast forms. We can now analyze the sequence differences that cause this variation of quaternary structure.
About this StructureAbout this Structure
1E58 is a Single protein structure of sequence from Escherichia coli. The following page contains interesting information on the relation of 1E58 with [The Glycolytic Enzymes]. Full crystallographic information is available from OCA.
ReferenceReference
High resolution structure of the phosphohistidine-activated form of Escherichia coli cofactor-dependent phosphoglycerate mutase., Bond CS, White MF, Hunter WN, J Biol Chem. 2001 Feb 2;276(5):3247-53. Epub 2000 Oct 18. PMID:11038361
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